O14526 (FCHO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
FCH domain only protein 1

Gene names

Name:	FCHO1
Synonyms:	KIAA0290

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	889 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. May regulate Bmp signaling by regulating clathrin-mediated endocytosis of Bmp receptors By similarity. Ref.8
Subunit structure	May oligomerize and form homotetramer By similarity. Interacts with AP2A2 and AP2B1; 2 subunits of the adaptor protein complex AP-2. Interacts with DAB2. Interacts with clathrin (CLTC or CLTCL1). Interacts with EPS15, EPS15R and ITSN1. Interacts with AGFG1 and CALM. May interact with ACVR1; linking this receptor to clathrin-mediated endocytosis. Ref.9
Subcellular location	Membrane › clathrin-coated pit; Peripheral membrane protein; Cytoplasmic side Probable. Note: Associated with forming but not mature clathrin-coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2. According to Ref.6 it may also dynamically associate with Golgi/TGN membranes. Ref.6 Ref.8
Sequence similarities	Belongs to the FCHO family. Contains 1 FCH domain. Contains 1 MUHD (Muniscin C-terminal mu homology domain) domain.
Sequence caution	The sequence BAA22959.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Coated pit Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	clathrin coat assembly Inferred from mutant phenotype Ref.8. Source: UniProtKB clathrin-mediated endocytosis Inferred from mutant phenotype Ref.8. Source: UniProtKB
Cellular_component	coated pit Inferred from direct assay Ref.8. Source: UniProtKB plasma membrane Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	AP-2 adaptor complex binding Inferred from direct assay Ref.9. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O14526-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O14526-2)

The sequence of this isoform differs from the canonical sequence as follows:
     883-889: GMYLVSC → AAPPQG

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 889	889	FCH domain only protein 1		PRO_0000271759
Regions
	Domain	2 – 83	82	FCH
	Domain	626 – 887	262	MUHD
	Region	1 – 275	275	Mediates membrane-binding
	Region	267 – 442	176	Mediates interaction with the adaptor protein complex AP-2
	Region	609 – 889	281	Mediates interaction with AGFG1, CALM, DAB2, EPS15, EPS15R, ITSN1 and clathrin
	Coiled coil	156 – 195	40	Potential
	Compositional bias	375 – 378	4	Poly-Ala
	Compositional bias	465 – 468	4	Poly-Ser
	Compositional bias	480 – 561	82	Pro-rich
	Compositional bias	671 – 674	4	Poly-Pro
Amino acid modifications
	Modified residue	182	1	Phosphotyrosine By similarity
	Modified residue	184	1	Phosphoserine By similarity
	Modified residue	616	1	Phosphoserine Ref.7
Natural variations
	Alternative sequence	883 – 889	7	GMYLVSC → AAPPQG in isoform 2.		VSP_022338

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 9, 2007. Version 2. Checksum: 8CDA1F24F42256D2	FASTA	889	96,861
	10 20 30 40 50 60 MSYFGEHFWG EKNHGFEVLY HSVKQGPIST KELADFIRER ATIEETYSKA MAKLSKLASN 70 80 90 100 110 120 GTPMGTFAPL WEVFRVSSDK LALCHLELTR KLQDLIKDVL RYGEEQLKTH KKCKEEVVST 130 140 150 160 170 180 LDAVQVLSGV SQLLPKSREN YLNRCMDQER LRRESTSQKE MDKAETKTKK AAESLRRSVE 190 200 210 220 230 240 KYNSARADFE QKMLDSALRF QAMEETHLRH MKALLGSYAH SVEDTHVQIG QVHEEFKQNI 250 260 270 280 290 300 ENVSVEMLLR KFAESKGTGR EKPGPLDFEA YSAAALQEAM KRLRGAKAFR LPGLSRRERE 310 320 330 340 350 360 PEPPAAVDFL EPDSGTCPEV DEEGFTVRPD VTQNSTAEPS RFSSSDSDFD DEEPRKFYVH 370 380 390 400 410 420 IKPAPARAPA CSPEAAAAQL RATAGSLILP PGPGGTMKRH SSRDAAGKPQ RPRSAPRTSS 430 440 450 460 470 480 CAERLQSEEQ VSKNLFGPPL ESAFDHEDFT GSSSLGFTSS PSPFSSSSPE NVEDSGLDSP 490 500 510 520 530 540 SHAAPGPSPD SWVPRPGTPQ SPPSCRAPPP EARGIRAPPL PDSPQPLASS PGPWGLEALA 550 560 570 580 590 600 GGDLMPAPAD PTAREGLAAP PRRLRSRKVS CPLTRSNGDL SRSLSPSPLG SSAASTALER 610 620 630 640 650 660 PSFLSQTGHG VSRGPSPVVL GSQDALPIAT AFTEYVHAYF RGHSPSCLAR VTGELTMTFP 670 680 690 700 710 720 AGIVRVFSGT PPPPVLSFRL VHTTAIEHFQ PNADLLFSDP SQSDPETKDF WLNMAALTEA 730 740 750 760 770 780 LQRQAEQNPT ASYYNVVLLR YQFSRPGPQS VPLQLSAHWQ CGATLTQVSV EYGYRPGATA 790 800 810 820 830 840 VPTPLTNVQI LLPVGEPVTN VRLQPAATWN LEEKRLTWRL PDVSEAGGSG RLSASWEPLS 850 860 870 880 GPSTPSPVAA QFTSEGTTLS GVDLELVGSG YRMSLVKRRF ATGMYLVSC
	Isoform 2 [UniParc]. Checksum: 27DB24B8191372A9	FASTA	888	96,629
	10 20 30 40 50 60 MSYFGEHFWG EKNHGFEVLY HSVKQGPIST KELADFIRER ATIEETYSKA MAKLSKLASN 70 80 90 100 110 120 GTPMGTFAPL WEVFRVSSDK LALCHLELTR KLQDLIKDVL RYGEEQLKTH KKCKEEVVST 130 140 150 160 170 180 LDAVQVLSGV SQLLPKSREN YLNRCMDQER LRRESTSQKE MDKAETKTKK AAESLRRSVE 190 200 210 220 230 240 KYNSARADFE QKMLDSALRF QAMEETHLRH MKALLGSYAH SVEDTHVQIG QVHEEFKQNI 250 260 270 280 290 300 ENVSVEMLLR KFAESKGTGR EKPGPLDFEA YSAAALQEAM KRLRGAKAFR LPGLSRRERE 310 320 330 340 350 360 PEPPAAVDFL EPDSGTCPEV DEEGFTVRPD VTQNSTAEPS RFSSSDSDFD DEEPRKFYVH 370 380 390 400 410 420 IKPAPARAPA CSPEAAAAQL RATAGSLILP PGPGGTMKRH SSRDAAGKPQ RPRSAPRTSS 430 440 450 460 470 480 CAERLQSEEQ VSKNLFGPPL ESAFDHEDFT GSSSLGFTSS PSPFSSSSPE NVEDSGLDSP 490 500 510 520 530 540 SHAAPGPSPD SWVPRPGTPQ SPPSCRAPPP EARGIRAPPL PDSPQPLASS PGPWGLEALA 550 560 570 580 590 600 GGDLMPAPAD PTAREGLAAP PRRLRSRKVS CPLTRSNGDL SRSLSPSPLG SSAASTALER 610 620 630 640 650 660 PSFLSQTGHG VSRGPSPVVL GSQDALPIAT AFTEYVHAYF RGHSPSCLAR VTGELTMTFP 670 680 690 700 710 720 AGIVRVFSGT PPPPVLSFRL VHTTAIEHFQ PNADLLFSDP SQSDPETKDF WLNMAALTEA 730 740 750 760 770 780 LQRQAEQNPT ASYYNVVLLR YQFSRPGPQS VPLQLSAHWQ CGATLTQVSV EYGYRPGATA 790 800 810 820 830 840 VPTPLTNVQI LLPVGEPVTN VRLQPAATWN LEEKRLTWRL PDVSEAGGSG RLSASWEPLS 850 860 870 880 GPSTPSPVAA QFTSEGTTLS GVDLELVGSG YRMSLVKRRF ATAAPPQG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins." Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N. DNA Res. 4:53-59(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Blood.
[6]	"Dynamic behavior of FCHO1 revealed by live-cell imaging microscopy: its possible involvement in clathrin-coated vesicle formation." Sakaushi S., Inoue K., Zushi H., Senda-Murata K., Fukada T., Oka S., Sugimoto K. Biosci. Biotechnol. Biochem. 71:1764-1768(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[8]	"FCHo proteins are nucleators of clathrin-mediated endocytosis." Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R., McMahon H.T. Science 328:1281-1284(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CLATHRIN-COATED PITS NUCLEATION, SUBCELLULAR LOCATION.
[9]	"Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning." Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M. Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract] Cited for: LIPID-BINDING, INTERACTION WITH ACVR1; AGFG1; AP2A2; AP2B1; CALM; DAB2; EPS15; EPS15R; ITSN1 AND CLATHRIN.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB006628 mRNA. Translation: BAA22959.1. Different initiation. AK291410 mRNA. Translation: BAF84099.1. AC008761 Genomic DNA. No translation available. CH471106 Genomic DNA. Translation: EAW84629.1. BC028021 mRNA. Translation: AAH28021.1. BC041130 mRNA. Translation: AAH41130.1.
IPI	IPI00182164. IPI00642769.
PIR	T00039.
RefSeq	NP_001154829.1. NM_001161357.1. NP_001154830.1. NM_001161358.1. NP_001154831.1. NM_001161359.1. NP_055937.1. NM_015122.2.
UniGene	Hs.96485.
3D structure databases
ProteinModelPortal	O14526.
ModBase	Search...
Protein-protein interaction databases
IntAct	O14526. 3 interactions.
STRING	9606.ENSP00000252771.
PTM databases
PhosphoSite	O14526.
Proteomic databases
PaxDb	O14526.
PRIDE	O14526.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000252771; ENSP00000252771; ENSG00000130475. ENST00000389133; ENSP00000373785; ENSG00000130475. ENST00000539407; ENSP00000437978; ENSG00000130475. ENST00000594202; ENSP00000473001; ENSG00000130475. ENST00000596536; ENSP00000470731; ENSG00000130475. ENST00000596951; ENSP00000472417; ENSG00000130475. ENST00000600676; ENSP00000470493; ENSG00000130475.
GeneID	23149.
KEGG	hsa:23149.
UCSC	uc002nhg.3. human. uc002nhh.2. human.
Organism-specific databases
CTD	23149.
GeneCards	GC19P017862.
HGNC	HGNC:29002. FCHO1.
HPA	HPA041653.
MIM	613437. gene.
neXtProt	NX_O14526.
PharmGKB	PA134870625.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG324072.
HOGENOM	HOG000231544.
HOVERGEN	HBG081524.
InParanoid	O14526.
OMA	ESAFDHE.
OrthoDB	EOG43XV31.
Gene expression databases
ArrayExpress	O14526.
Bgee	O14526.
CleanEx	HS_FCHO1.
Genevestigator	O14526.
Family and domain databases
InterPro	IPR001060. FCH_dom. IPR018808. Muniscin_C-term_mu_dom. [Graphical view]
Pfam	PF00611. FCH. 1 hit. PF10291. muHD. 1 hit. [Graphical view]
SMART	SM00055. FCH. 1 hit. [Graphical view]
PROSITE	PS50133. FCH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	FCHO1. human.
GenomeRNAi	23149.
NextBio	44466.
SOURCE	Search...

Entry information

Entry name

FCHO1_HUMAN

Accession

Primary (citable) accession number: O14526
Secondary accession number(s): A6NHE6 , A8K5U5, Q05C93, Q8IW22

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	January 9, 2007
Last modified:	May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.